Separation of pepsin I, pepsin II A, pepsin II B, and pepsin III from human gastric mucosa

Seijffers, Max J.; Segal, Harry L.; Miller, Leon L.

doi:10.1152/ajplegacy.1963.205.6.1099

Cited by 93 publications

(9 citation statements)

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“…No difference in heat inactivation was observed between PI and PII. These findings differ from the results of Seijffers et al who found their pepsin I (PII) more heat-resistant than other pepsins [14].…”

Section: Discussioncontrasting

confidence: 93%

“…During alkali activation PII proved to be more stable than porc pepsin and PI. These differences in stability have already been observed and used for the separate enzymatic determination of those pepsins [14,15]. No difference in heat inactivation was observed between PI and PII.…”

Section: Discussionmentioning

confidence: 59%

“…Gastricsin was later associated with the active form of PgII [10]. An identical pepsin (pepsin I) was purified from gastric juice by Seijffers [14] which might as well be comparable to the active form of PgII.…”

mentioning

confidence: 99%

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Characterization of human pepsin II obtained from purified gastric pepsinogen II

Becker

Rapp

1979

Klin Wochenschr

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Human pepsinogen II (PgII) was purified from human gastric mucosa by immunoadsorbents using anti-PgII antiserum. Contaminating pepsinogen I (PgI) was adsorbed by a subsequent anti-PgI immunoadsorbent. PgII was further purified on DEAE-Sphadex A50. By agar gel enzyme electrophoresis (AEE) at pH 8.2 PgII was separated into five proteolytic bands, demonstrated upon acidification and incubation with hemoglobin. PgII was converted to pepsin II (PII) by acidification at pH 2.0 and was immediately separated from its inhibitory peptide and from other substances by DEAE chromatography. Purified PII showed two bands in AEE at pH 5.6 and was immunochemically identical with PgII. The "gastricsin" and "pepsin" purified from acid gastric juice by classical procedures proved to be identical with PII and pepsin I (PI), respectively. PII showed a broad pH range with one maximum at pH 2.9. PII in contrast to PI did not hydrolize N-acetylphenylalanyl-3,5-diiodotyrosine and proved to be more alkali-stable than PI. A modified nomenclature is proposed for the human pepsinogen system.

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Section: Discussioncontrasting

confidence: 93%

Section: Discussionmentioning

confidence: 59%

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Characterization of human pepsin II obtained from purified gastric pepsinogen II

Becker

Rapp

1979

Klin Wochenschr

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“…Human gastric juice contains several pepsins [9] and there is some evidence to suggest that pepsin I may be the most important of these in the peptic ulcer diathesis [10,13]. On the other hand, it must be pointed out that the various authorities use widely varying methods of measuring the pepsin I fraction and that there is no international agreement as to its identity.…”

Section: Discussionmentioning

confidence: 99%

Acid and Pepsin Dose-Response Studies to Insulin Hypoglycaemia in a Healthy Man

Wilson¹,

Dymock²,

Cowley³

1974

Digestion

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The relationship between the secretion of acid and pepsin and degree of hypoglycaemia has been studied in response to five doses of insulin (0.0125–0.2 U/kg) given by intravenous injection in a healthy man. Two tests were carried out at each dose. Both peak acid aoutput (PAO_I) and peak pepsin output (PPO_I) increased with the logarithm of the dose of insulin up to 0.2 U/kg. There was a significant inverse correlation between the lowest blood glucose attained and both PAO_I (r = -0.81, p < 0.01) and PPO_I (r = -0.77, p < 0.01). Acid and pepsin output increased in parallel in relation to both the dose of insulin and the degree of hypoglycaemia. The relationship between pepsin I and total pepsin was constant for all levels of acid secretion. Inhibition of secretion was not observed with the lowest levels of hypoglycaemia attained. In health, insulin hypoglycaemia provides a quantitative glycopenic stimulus which produces a quantitative and parallel response for both acid and pepsin.

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“…One unit of activity was defined as the amount which caused an increase of 1 Aase/min under the above conditions. Milk clotting activity was measured as in [7] . Protein was determined as in [8] using bovine serum albumin as a standard.…”

Section: Methodsmentioning

confidence: 99%